ArticleCellular signalling2010
Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors.
Article in Cellular signalling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Potential involvement of IL-32 in cell-to-cell communication between macrophages and hepatoblastoma.Pediatric surgery international · 2023Article
- Allosteric modulation of gonadotropin receptors.Frontiers in endocrinology · 2023Review
- Human FSH Glycoform α-Subunit AsparagineFrontiers in endocrinology · 2022Article
- Targeting trafficking as a therapeutic avenue for misfolded GPCRs leading to endocrine diseases.Frontiers in endocrinology · 2022Review
- A Novel Follitropin Analog Inhibits Follitropin Activity In Vitro.Pharmaceutics · 2021Article
- Differential FSH Glycosylation Modulates FSHR Oligomerization and Subsequent cAMP Signaling.Frontiers in endocrinology · 2021Article
- Receptor-Receptor Interactions as a Widespread Phenomenon: Novel Targets for Drug Development?Frontiers in endocrinology · 2019Review
- Molecular and functional insights into gonadotropin hormone receptor dimerization and oligomerization.Minerva ginecologica · 2018Review
- Temporal reprogramming of calcium signalling via crosstalk of gonadotrophin receptors that associate as functionally asymmetric heteromers.Scientific reports · 2018Article
- FSHR Trans-Activation and Oligomerization.Frontiers in endocrinology · 2018Review
- Structure-Function Relationships of the Follicle-Stimulating Hormone Receptor.Frontiers in endocrinology · 2018Review
- Misfolding Ectodomain Mutations of the Lutropin Receptor Increase Efficacy of Hormone Stimulation.Molecular endocrinology (Baltimore, Md.) · 2016Article
- Production, purification, and characterization of recombinant hFSH glycoforms for functional studies.Molecular and cellular endocrinology · 2015Article
- Single molecule analysis of functionally asymmetric G protein-coupled receptor (GPCR) oligomers reveals diverse spatial and structural assemblies.The Journal of biological chemistry · 2015Article
- Discovery and Development of Small Molecule Allosteric Modulators of Glycoprotein Hormone Receptors.Frontiers in endocrinology · 2015Review
- Follicle-stimulating hormone receptor (FSHR) alternative skipping of exon 2 or 3 affects ovarian response to FSH.Molecular human reproduction · 2014Article
- Hypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24)).Molecular and cellular endocrinology · 2014Article
- Mutations in G protein-coupled receptors that impact receptor trafficking and reproductive function.Molecular and cellular endocrinology · 2014Review
- Novel insights on thyroid-stimulating hormone receptor signal transduction.Endocrine reviews · 2013Review
- Heterodimerization between the lutropin and follitropin receptors is associated with an attenuation of hormone-dependent signaling.Endocrinology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The human follitropin receptor (hFSHR) is a G protein-coupled receptor (GPCR) central to reproductive physiology that is composed of an extracellular domain (ECD) fused to a serpentine region. Using bioluminescence resonance energy transfer (BRET) in living cells, we show that hFSHR dimers form constitutively during their biosynthesis. Mutations in TM1 and TM4 had no effect on hFSHR dimerization, alone or when combined with mutation of Tyr(110) in the ECD, a residue predicted to mediate dimerization of the soluble hormone-binding portion of the ECD complexed with FSH (Q. Fan and W. Hendrickson, Nature 433:269-277, 2005). Expressed individually, the serpentine region and a membrane-anchored form of the hFSHR ECD each exhibited homodimerization, suggesting that both domains contribute to dimerization of the full-length receptor. However, even in the context of only the membrane-anchored ECD, mutation of Tyr(110) to alanine did not inhibit dimerization. The full-length hFSHR and the membrane-anchored ECD were then each engineered to introduce a consensus site for N-linked glycosylation at residue 110. Despite experimental validation of the presence of carbohydrate on residue 110, we failed to observe disruption of dimerization of either the full-length hFSHR or membrane-anchored ECD containing the inserted glycan wedge. Taken altogether, our data suggest that both the serpentine region and the ECD contribute to hFSHR dimerization and that the dimerization interface of the unoccupied hFSHR does not involve Tyr(110) of the ECD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.